Classifications

• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
  • A61L15/00—Chemical aspects of, or use of materials for, bandages, dressings or absorbent pads
  • A61L15/16—Bandages, dressings or absorbent pads for physiological fluids such as urine or blood, e.g. sanitary towels, tampons
  • A61L15/22—Bandages, dressings or absorbent pads for physiological fluids such as urine or blood, e.g. sanitary towels, tampons containing macromolecular materials
  • A61L15/32—Proteins, polypeptides; Degradation products or derivatives thereof, e.g. albumin, collagen, fibrin, gelatin
  • A61L15/325—Collagen
• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
  • A61L15/00—Chemical aspects of, or use of materials for, bandages, dressings or absorbent pads
  • A61L15/16—Bandages, dressings or absorbent pads for physiological fluids such as urine or blood, e.g. sanitary towels, tampons
  • A61L15/22—Bandages, dressings or absorbent pads for physiological fluids such as urine or blood, e.g. sanitary towels, tampons containing macromolecular materials
  • A61L15/225—Mixtures of macromolecular compounds

Definitions

• Collagen has been used in surgery for some time. It can be used in the form of sponges or fibers to control bleeding and, properly modified, is suited also to promote the healing of wounds.
• the usual collagenous dressings are inadequate. Attempts have therefore been made to bond collagenous material, such as collagen or gelatin, to tissue by the use of adhesives based on resorcinol-formaldehyde. While such adhesives are hemostatic, they are not suited for practical use because of their tissue irritation. This is true also of acrylate adhesives and their combination with collagenous dressings.
• collagen in the body is crosslinked with constituents of connective tissue.
• collagen is crosslinked through Schiff bases and aldol condensation.
• tissue strength is enhanced through disulfide bridges of the basal membrane collagen.
• crosslink proteins such as albumin with intermolecular disulfide bonds through disulfide bridges after mild reduction followed by oxidation.
• blood clotting forms a primary closure of the wound. This is due to aggregated thrombocytes and a fibrin network during the end phase of the plasmatic coagulation.
• individual fibrin molecules are crosslinked through transglutaminase.
• the fibrinogen component of the three components is often not available at the critical moment in a form ready for use since at least the deep-frozen fibrinogen solution must first be thawed. Moreover, mixing prior to application is relatively complicated.
• the object of the invention is to provide a collagenous dressing which will conglutinate with (ie. adhere to) the tissue and which does not have the known drawbacks of fibrin bonding in combination with resorbable collagen. Coupled with this object is an improvement to collagenous dressings for local hemostasis.
• tissue-adherent collagenous dressing which is characterized in that it contains collagen in combination with a resorbable biopolymer from the group comprising fibrinogen, gelatin modified to contain SH groups, collagen modified to contain SH groups, or oxycellulose modified to contain SH groups.
• Collagen and fibrinogen or the gelatin modified by SH groups similarly modified collagen or similarly modified oxycellulose may advantageously be combined with each other through freeze drying.
• SH groups it is also possible to introduce SH groups into the collagen.
• fibrinogen here takes the place of said resorbable biopolymers, namely, gelatin modified to contain SH groups, collagen modified to contain SH groups, or oxycellulose modified to contain SH groups.
• biopolymers containing reactive SH groups are gelatin modified to contain SH groups, regenerated oxycellulose modified to contain SH groups, or collagen modified to contain SH groups.
• SH groups into collagen may be effected in a manner which per se is known. For example, the procedure set forth by Benesch & Benesch in "Proceedings of the National Academy of the United States, Washington, D.C.”, vol. 44 (1958), pp. 848-853, may be followed.
• SH groups can also be introduced into collagen by depositing a gelatin modified by SH groups, or a similarly modified regenerated oxycellulose, on collagen or mixing it therewith by means of a gradient mixer.
• Gelatin is formed from collagen through chemical or enzymatic decomposition and thus has the same chemical composition. Consequently, collagenous dressings provided with gelatin modified to contain SH groups essentially also have the properties of collagen along with the advantage that because of the SH groups in these materials oxidative crosslinking is able to occur.
• the collagenous dressings in accordance with the invention may incorporate active substances, in a manner which is known per se.
• the collagen used as a dressing has the usual form of dressings, i.e., gauze, cloth, sponge, etc.
• the purity of the collagen used is less than 4, and preferably less than 3. Since hydroxyproline occurs only in collagen, this is a measure for the purity of the collagen.
• the resorbable biopolymer is present in the tissue-adherent collagenous dressing in an amount ranging from 0.5 to 10 mg/cm 2 , and preferably from 4 to 6 mg/cm 2 .
• the number of SH groups per molecule of resorbable biopolymer may vary over a wide range. For gelatin of an average molecular weight of about 40,000 it is about 2 to 7 and on the average about 5, and for the other resorbable biopolymers it is of the same order of magnitude.
• collagen is suitable for use as a vehicle for antibiotics such as gentamycin. Tetracycline or other antibiotics or chemotherapeutic agents may also be worked into the collagen modified to contain SH groups. This is an additional effect that can be obtained with the dressings in accordance with the invention.
• the tissue suspended in 3 liters 1% acetic acid, was incubated for 48 hours at 15° C. with constant stirring, with pepsin in a collagen-to-pepsin ratio of 50:1.
• the batch was diluted with 1% acetic acid to 5 liters and freed of undissolved tendom fragments by centrifugation.
• the viscous collagen solution was dialyzed against alkalinized tap water (pH 8.0) and then vigorously centrifuged. The residue was again dissolved in 5 liters 1% acetic acid and dialyzed. This procedure was repeated until the nitrogen-to-hydroxyproline ratio was less than 3. After the last dialysis, a 1.5% collagen solution was prepared by means of 0.05% acetic acid, which was then used in the tests described below.
• the regenerated oxycellulose was dehydrated by lyophilization.
• gentamycin-containing dressings For the preparation of gentamycin-containing dressings, 100 mg gentamycin was added to 100 ml of a 1% collagen solution, and this solution was used as described above to prepare a collagen/fibrinogen-containing dressing and a collagen/SH-gelatin-containing dressing.
• modified tissue-agglutinable collagenous dressings in accordance with the invention, resorption occurs within clinically appropriate periods of time.
• they can be used to dress even large-area wounds, especially in the abdominal region.

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• Health & Medical Sciences (AREA)
• Hematology (AREA)
• Chemical & Material Sciences (AREA)
• Engineering & Computer Science (AREA)
• Materials Engineering (AREA)
• Epidemiology (AREA)
• Life Sciences & Earth Sciences (AREA)
• Animal Behavior & Ethology (AREA)
• General Health & Medical Sciences (AREA)
• Public Health (AREA)
• Veterinary Medicine (AREA)
• Materials For Medical Uses (AREA)
• Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
• Medicinal Preparation (AREA)

Applications Claiming Priority (2)

Publications (1)

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Cited By (75)

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Citations (3)

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• 1980
  • 1980-10-03 DE DE3037513A patent/DE3037513C2/de not_active Expired
• 1981
  • 1981-09-21 US US06/303,851 patent/US4407787A/en not_active Expired - Lifetime
  • 1981-09-25 CA CA000386640A patent/CA1167726A/en not_active Expired
  • 1981-09-30 AT AT81107775T patent/ATE5373T1/de not_active IP Right Cessation
  • 1981-09-30 EP EP81107775A patent/EP0049469B2/de not_active Expired
  • 1981-09-30 DE DE8181107775T patent/DE3161508D1/de not_active Expired
  • 1981-10-02 JP JP56156320A patent/JPS5841559A/ja active Granted
• 1986
  • 1986-07-17 HK HK534/86A patent/HK53486A/xx not_active IP Right Cessation

Patent Citations (3)

Non-Patent Citations (2)

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